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Peroxiredoxin-5, mitochondrial (EC 1.11.1.15) (Alu corepressor 1) (Antioxidant enzyme B166) (AOEB166) (Liver tissue 2D-page spot 71B) (PLP) (Peroxiredoxin V) (Prx-V) (Peroxisomal antioxidant enzyme) (TPx type VI) (Thioredoxin peroxidase PMP20)

 PRDX5_HUMAN             Reviewed;         214 AA.
P30044; A6NC19; A6NG06; B7ZLJ4; B7ZVW3; Q14CK0; Q6IAF2; Q9UBU5;
Q9UJU4; Q9UKX4;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
25-OCT-2017, entry version 190.
RecName: Full=Peroxiredoxin-5, mitochondrial;
EC=1.11.1.15 {ECO:0000269|PubMed:10751410};
AltName: Full=Alu corepressor 1;
AltName: Full=Antioxidant enzyme B166;
Short=AOEB166;
AltName: Full=Liver tissue 2D-page spot 71B;
AltName: Full=PLP;
AltName: Full=Peroxiredoxin V;
Short=Prx-V;
AltName: Full=Peroxisomal antioxidant enzyme;
AltName: Full=TPx type VI;
AltName: Full=Thioredoxin peroxidase PMP20;
Flags: Precursor;
Name=PRDX5; Synonyms=ACR1; ORFNames=SBBI10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), AND VARIANT
CYS-33.
PubMed=10095767; DOI=10.1046/j.1432-1327.1999.00162.x;
Kropotov A., Sedova V., Ivanov V., Sazeeva N., Tomilin A.,
Krutilina R., Oei S.L., Griesenbeck J., Buchlow G., Tomilin N.;
"A novel human DNA-binding protein with sequence similarity to a
subfamily of redox proteins which is able to repress RNA-polymerase-
III-driven transcription of the Alu-family retroposons in vitro.";
Eur. J. Biochem. 260:336-346(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL),
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10514471; DOI=10.1074/jbc.274.42.29897;
Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P.,
Subramani S., Rogers R.A., Avraham H.;
"Characterization of human and murine PMP20 peroxisomal proteins that
exhibit antioxidant activity in vitro.";
J. Biol. Chem. 274:29897-29904(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), PROTEIN SEQUENCE
OF 54-90, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
VARIANT CYS-33.
TISSUE=Lung;
PubMed=10521424; DOI=10.1074/jbc.274.43.30451;
Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C.,
Duconseille E., Falmagne P., Bernard A.;
"Cloning and characterization of AOEB166, a novel mammalian
antioxidant enzyme of the peroxiredoxin family.";
J. Biol. Chem. 274:30451-30458(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), AND
VARIANT CYS-33.
PubMed=10679306; DOI=10.1006/bbrc.2000.2231;
Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M.,
Fung P.C.W., Kung H.-F., Jin D.-Y.;
"Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-
induced apoptosis.";
Biochem. Biophys. Res. Commun. 268:921-927(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
OF CYS-100; CYS-125 AND CYS-204, ACTIVE SITE, DISULFIDE BOND, AND
SUBCELLULAR LOCATION.
PubMed=10751410; DOI=10.1074/jbc.M001943200;
Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G.;
"Identification of a new type of mammalian peroxiredoxin that forms an
intramolecular disulfide as a reaction intermediate.";
J. Biol. Chem. 275:20346-20354(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
Kim I.H., Jeong W.;
"A new type of human thiol peroxidase (Human TPx type VI).";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), AND VARIANT
CYS-33.
Zhang W., Li N., Wan T., Cao X.;
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM
CYTOPLASMIC+PEROXISOMAL).
TISSUE=Adrenal gland;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MITOCHONDRIAL), AND
VARIANT CYS-33.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT CYS-33.
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MITOCHONDRIAL; 3 AND
4), AND VARIANT CYS-33.
TISSUE=Brain, and Medulla oblongata;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
PROTEIN SEQUENCE OF 54-63.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed=11518528; DOI=10.1006/jmbi.2001.4853;
Declercq J.-P., Evrard C., Clippe A., Stricht D.V., Bernard A.,
Knoops B.;
"Crystal structure of human peroxiredoxin 5, a novel type of mammalian
peroxiredoxin at 1.5-A resolution.";
J. Mol. Biol. 311:751-759(2001).
[19]
X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 54-214, AND DISULFIDE BOND.
PubMed=18489898; DOI=10.1016/j.abb.2008.04.036;
Smeets A., Marchand C., Linard D., Knoops B., Declercq J.P.;
"The crystal structures of oxidized forms of human peroxiredoxin 5
with an intramolecular disulfide bond confirm the proposed enzymatic
mechanism for atypical 2-Cys peroxiredoxins.";
Arch. Biochem. Biophys. 477:98-104(2008).
[20]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 54-214 IN COMPLEX WITH
DITHIOTHREITOL, AND ACTIVE SITE.
PubMed=20643143; DOI=10.1016/j.jmb.2010.07.022;
Hall A., Parsonage D., Poole L.B., Karplus P.A.;
"Structural evidence that peroxiredoxin catalytic power is based on
transition-state stabilization.";
J. Mol. Biol. 402:194-209(2010).
[21]
VARIANT [LARGE SCALE ANALYSIS] LEU-157.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events.
{ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10521424,
ECO:0000269|PubMed:10751410}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:10751410}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20643143}.
-!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion
{ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410}.
-!- SUBCELLULAR LOCATION: Isoform Cytoplasmic+peroxisomal: Cytoplasm
{ECO:0000269|PubMed:10514471, ECO:0000269|PubMed:10751410}.
Peroxisome matrix {ECO:0000269|PubMed:10514471,
ECO:0000269|PubMed:10521424, ECO:0000269|PubMed:10751410}.
Note=Imported into peroxisomes via peroxisomal targeting signal 1
receptor PEX5. {ECO:0000269|PubMed:10514471}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=4;
Name=Mitochondrial;
IsoId=P30044-1; Sequence=Displayed;
Name=Cytoplasmic+peroxisomal;
IsoId=P30044-2; Sequence=VSP_018829;
Name=3;
IsoId=P30044-3; Sequence=VSP_045783;
Note=No experimental confirmation available.;
Name=4;
IsoId=P30044-4; Sequence=VSP_046682;
Note=Produced by alternative splicing.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10521424}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this atypical 2-Cys Prx, C(R) is present in the same
subunit to form an intramolecular disulfide. The disulfide is
subsequently reduced by thioredoxin. {ECO:0000305|PubMed:10751410,
ECO:0000305|PubMed:18489898}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF17200.1; Type=Frameshift; Positions=14, 30; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/prdx5/";
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EMBL; AF231705; AAF78899.1; -; mRNA.
EMBL; AF124993; AAF27531.1; -; mRNA.
EMBL; AF110731; AAF03750.1; -; mRNA.
EMBL; AF197952; AAF04856.1; -; mRNA.
EMBL; AJ249483; CAB62210.1; -; mRNA.
EMBL; AF242525; AAF99605.1; -; mRNA.
EMBL; AF112212; AAF17200.1; ALT_FRAME; mRNA.
EMBL; CR457203; CAG33484.1; -; mRNA.
EMBL; DQ247769; ABB05181.1; -; Genomic_DNA.
EMBL; AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC110983; AAI10984.1; -; mRNA.
EMBL; BC113723; AAI13724.1; -; mRNA.
EMBL; BC113725; AAI13726.1; -; mRNA.
EMBL; BC143849; AAI43850.1; -; mRNA.
EMBL; BC171733; AAI71733.1; -; mRNA.
CCDS; CCDS8069.1; -. [P30044-1]
CCDS; CCDS8070.1; -. [P30044-3]
CCDS; CCDS8071.1; -. [P30044-4]
RefSeq; NP_036226.1; NM_012094.4.
RefSeq; NP_857634.1; NM_181651.2.
RefSeq; NP_857635.1; NM_181652.2.
UniGene; Hs.502823; -.
PDB; 1H4O; X-ray; 1.95 A; A/B/C/D/E/F/G/H=54-214.
PDB; 1HD2; X-ray; 1.50 A; A=54-214.
PDB; 1OC3; X-ray; 2.00 A; A/B/C=54-214.
PDB; 1URM; X-ray; 1.70 A; A=54-214.
PDB; 2VL2; X-ray; 1.92 A; A/B/C=54-214.
PDB; 2VL3; X-ray; 1.83 A; A/B/C=54-214.
PDB; 2VL9; X-ray; 2.70 A; A/B/C/D=54-214.
PDB; 3MNG; X-ray; 1.45 A; A=54-214.
PDB; 4K7I; X-ray; 2.25 A; A/B/C=54-214.
PDB; 4K7N; X-ray; 2.30 A; A/B/C=54-214.
PDB; 4K7O; X-ray; 1.98 A; A/B/C=54-214.
PDB; 4MMM; X-ray; 1.47 A; A/C/E/G=54-214.
PDBsum; 1H4O; -.
PDBsum; 1HD2; -.
PDBsum; 1OC3; -.
PDBsum; 1URM; -.
PDBsum; 2VL2; -.
PDBsum; 2VL3; -.
PDBsum; 2VL9; -.
PDBsum; 3MNG; -.
PDBsum; 4K7I; -.
PDBsum; 4K7N; -.
PDBsum; 4K7O; -.
PDBsum; 4MMM; -.
ProteinModelPortal; P30044; -.
SMR; P30044; -.
BioGrid; 117352; 80.
IntAct; P30044; 29.
MINT; MINT-5002532; -.
STRING; 9606.ENSP00000265462; -.
ChEMBL; CHEMBL3627586; -.
DrugBank; DB00995; Auranofin.
DrugBank; DB03793; Benzoic Acid.
DrugBank; DB03608; Diminazene.
PeroxiBase; 4448; HsPrxV.
iPTMnet; P30044; -.
PhosphoSitePlus; P30044; -.
SwissPalm; P30044; -.
BioMuta; PRDX5; -.
DMDM; 317373539; -.
OGP; P30044; -.
REPRODUCTION-2DPAGE; IPI00759663; -.
SWISS-2DPAGE; P30044; -.
UCD-2DPAGE; P30044; -.
EPD; P30044; -.
MaxQB; P30044; -.
PaxDb; P30044; -.
PeptideAtlas; P30044; -.
PRIDE; P30044; -.
TopDownProteomics; P30044-1; -. [P30044-1]
TopDownProteomics; P30044-2; -. [P30044-2]
DNASU; 25824; -.
Ensembl; ENST00000265462; ENSP00000265462; ENSG00000126432. [P30044-1]
Ensembl; ENST00000347941; ENSP00000335363; ENSG00000126432. [P30044-4]
Ensembl; ENST00000352435; ENSP00000335334; ENSG00000126432. [P30044-3]
GeneID; 25824; -.
KEGG; hsa:25824; -.
UCSC; uc001nzu.4; human. [P30044-1]
CTD; 25824; -.
DisGeNET; 25824; -.
EuPathDB; HostDB:ENSG00000126432.13; -.
GeneCards; PRDX5; -.
HGNC; HGNC:9355; PRDX5.
HPA; CAB008661; -.
HPA; HPA037915; -.
HPA; HPA037916; -.
MIM; 606583; gene.
neXtProt; NX_P30044; -.
OpenTargets; ENSG00000126432; -.
PharmGKB; PA33726; -.
eggNOG; KOG0541; Eukaryota.
eggNOG; COG0678; LUCA.
GeneTree; ENSGT00390000018173; -.
HOGENOM; HOG000255884; -.
HOVERGEN; HBG053675; -.
InParanoid; P30044; -.
KO; K11187; -.
OMA; QRYAMVV; -.
OrthoDB; EOG091G0OSA; -.
PhylomeDB; P30044; -.
TreeFam; TF105182; -.
BRENDA; 1.11.1.15; 2681.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
SIGNOR; P30044; -.
ChiTaRS; PRDX5; human.
EvolutionaryTrace; P30044; -.
GeneWiki; PRDX5; -.
GenomeRNAi; 25824; -.
PRO; PR:P30044; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000126432; -.
CleanEx; HS_PRDX5; -.
Genevisible; P30044; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0004601; F:peroxidase activity; IDA:UniProtKB.
GO; GO:0051920; F:peroxiredoxin activity; IDA:UniProtKB.
GO; GO:0072541; F:peroxynitrite reductase activity; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0001016; F:RNA polymerase III regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0008379; F:thioredoxin peroxidase activity; EXP:Reactome.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0070995; P:NADPH oxidation; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0051354; P:negative regulation of oxidoreductase activity; IDA:UniProtKB.
GO; GO:0016480; P:negative regulation of transcription from RNA polymerase III promoter; IDA:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB.
GO; GO:2001057; P:reactive nitrogen species metabolic process; IDA:UniProtKB.
GO; GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; IDA:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
InterPro; IPR013740; Redoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF08534; Redoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation;
Alternative splicing; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Mitochondrion;
Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein; Polymorphism;
Redox-active center; Reference proteome; Transit peptide.
TRANSIT 1 52 Mitochondrion. {ECO:0000255}.
CHAIN 53 214 Peroxiredoxin-5, mitochondrial.
/FTId=PRO_0000023793.
DOMAIN 56 214 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 212 214 Microbody targeting signal.
{ECO:0000305|PubMed:10514471}.
ACT_SITE 100 100 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000305|PubMed:10751410,
ECO:0000305|PubMed:20643143}.
MOD_RES 75 75 N6-acetyllysine.
{ECO:0000250|UniProtKB:P99029}.
MOD_RES 83 83 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 83 83 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P99029}.
MOD_RES 116 116 N6-succinyllysine.
{ECO:0000250|UniProtKB:P99029}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R063}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000250|UniProtKB:P99029}.
DISULFID 100 204 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691,
ECO:0000269|PubMed:10751410,
ECO:0000269|PubMed:18489898}.
VAR_SEQ 1 52 Missing (in isoform
Cytoplasmic+peroxisomal).
{ECO:0000303|PubMed:10514471,
ECO:0000303|PubMed:10679306,
ECO:0000303|PubMed:10931946,
ECO:0000303|Ref.6}.
/FTId=VSP_018829.
VAR_SEQ 57 145 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046682.
VAR_SEQ 102 145 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045783.
VARIANT 33 33 Y -> C (in dbSNP:rs7938623).
{ECO:0000269|PubMed:10095767,
ECO:0000269|PubMed:10521424,
ECO:0000269|PubMed:10679306,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.10, ECO:0000269|Ref.7,
ECO:0000269|Ref.9}.
/FTId=VAR_025049.
VARIANT 157 157 F -> L (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036406.
MUTAGEN 100 100 C->S: Complete loss of activity.
{ECO:0000269|PubMed:10751410}.
MUTAGEN 125 125 C->S: No change in activity.
{ECO:0000269|PubMed:10751410}.
MUTAGEN 204 204 C->S: Complete loss of activity.
{ECO:0000269|PubMed:10751410}.
CONFLICT 141 141 H -> T (in Ref. 4; AAF04856).
{ECO:0000305}.
STRAND 66 68 {ECO:0000244|PDB:3MNG}.
HELIX 72 74 {ECO:0000244|PDB:2VL9}.
STRAND 75 77 {ECO:0000244|PDB:3MNG}.
HELIX 78 81 {ECO:0000244|PDB:3MNG}.
TURN 82 84 {ECO:0000244|PDB:3MNG}.
STRAND 85 91 {ECO:0000244|PDB:3MNG}.
HELIX 98 102 {ECO:0000244|PDB:3MNG}.
HELIX 104 110 {ECO:0000244|PDB:3MNG}.
HELIX 112 116 {ECO:0000244|PDB:3MNG}.
TURN 117 119 {ECO:0000244|PDB:3MNG}.
STRAND 122 129 {ECO:0000244|PDB:3MNG}.
HELIX 131 140 {ECO:0000244|PDB:3MNG}.
TURN 144 146 {ECO:0000244|PDB:3MNG}.
STRAND 148 151 {ECO:0000244|PDB:3MNG}.
HELIX 156 161 {ECO:0000244|PDB:3MNG}.
HELIX 167 169 {ECO:0000244|PDB:4MMM}.
HELIX 170 173 {ECO:0000244|PDB:3MNG}.
STRAND 181 186 {ECO:0000244|PDB:3MNG}.
STRAND 189 195 {ECO:0000244|PDB:3MNG}.
STRAND 199 203 {ECO:0000244|PDB:4MMM}.
HELIX 207 213 {ECO:0000244|PDB:3MNG}.
SEQUENCE 214 AA; 22086 MW; DA1DEB21120254EE CRC64;
MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRYSEGEWAS GGVRSFSRAA AAMAPIKVGD
AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKTHLPGFVE QAEALKAKGV
QVVACLSVND AFVTGEWGRA HKAEGKVRLL ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR
FSMVVQDGIV KALNVEPDGT GLTCSLAPNI ISQL


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